1887

Abstract

can bind to saliva-coated tooth surfaces. However, the nature of the domains of salivary protein that interact with remains unclear. The ability of individual proteins in human submandibular-sublingual saliva (HSMSL) to bind cells was examined by dot blot assay; statherin displayed the strongest binding activity. Statherin binding sites were determined based on binding of I-labelled to statherin-coated hydroxyapatite (sHAP) beads via inhibition assays using synthetic analogous peptide fragments of whole statherin. Analogous peptides corresponding to residues 19–26 and 32–39 of statherin inhibited binding by 77 % and 68 %, respectively. Synthetic peptides were also prepared by serial deletions of individual residues from N- and C-termini of the peptides GPYQPVPE (aa 19–26) and QPYQPQYQ (aa 32–39). The inhibitory effects of peptides YQPVPE (aa 21–26) and PYQPQYQ (aa 33–39) were very similar to those of GPYQPVPE and QPYQPQYQ, respectively. However, additional deletion of residues resulted in significant reduction of the inhibitory effect. Alanine-scan analysis of YQPVPE revealed that all tested peptides retained inhibitory activity; only YPVPE exhibited significantly decreased inhibitory activity. These findings suggest that YQPVPE and PYQPQYQ may represent the minimal active segments of statherin for binding to ; moreover, Gln may be a key amino acid in the active segment.

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2004-07-01
2019-10-17
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